NUP93_MOUSE
ID NUP93_MOUSE Reviewed; 819 AA.
AC Q8BJ71; Q3TED9; Q8BIK7; Q8K1R4; Q8R592;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Nuclear pore complex protein Nup93;
DE AltName: Full=93 kDa nucleoporin;
DE AltName: Full=CBP-interacting protein 4;
DE AltName: Full=Nucleoporin Nup93;
GN Name=Nup93; Synonyms=Cip4, Kiaa0095;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain, Skin, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 1-163 (ISOFORM 1).
RA Heery D.M., Harries J.C., Kindle K.B., Viskaduraki M., Matsuda S.,
RA Sheppard H.M., Davis A.;
RT "Diverse nuclear proteins compete with SRC1 for interaction with CREB
RT binding protein.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=26878725; DOI=10.1038/ng.3512;
RA Braun D.A., Sadowski C.E., Kohl S., Lovric S., Astrinidis S.A., Pabst W.L.,
RA Gee H.Y., Ashraf S., Lawson J.A., Shril S., Airik M., Tan W., Schapiro D.,
RA Rao J., Choi W.I., Hermle T., Kemper M.J., Pohl M., Ozaltin F., Konrad M.,
RA Bogdanovic R., Buescher R., Helmchen U., Serdaroglu E., Lifton R.P.,
RA Antonin W., Hildebrandt F.;
RT "Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause steroid-
RT resistant nephrotic syndrome.";
RL Nat. Genet. 48:457-465(2016).
CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
CC and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to
CC the NPC (By similarity). During renal development, regulates podocyte
CC migration and proliferation through SMAD4 signaling (By similarity)
CC (PubMed:26878725). {ECO:0000250|UniProtKB:Q8N1F7,
CC ECO:0000269|PubMed:26878725}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). Component of the p62
CC complex, a complex composed of NUP62 and NUP54. Forms a complex with
CC NUP35, NUP155, NUP205 and lamin B; the interaction with NUP35 is
CC direct. Does not interact with TPR. Interacts with SMAD4 and IPO7;
CC translocates SMAD4 to the nucleus through the NPC upon BMP7 stimulation
CC resulting in activation of SMAD4 signaling.
CC {ECO:0000250|UniProtKB:Q8N1F7}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q66HC5};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q66HC5}. Nucleus,
CC nuclear pore complex {ECO:0000250|UniProtKB:Q8N1F7}. Nucleus envelope
CC {ECO:0000269|PubMed:26878725}. Note=Localizes at the nuclear basket and
CC at or near the nuclear entry to the gated channel of the pore.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BJ71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJ71-2; Sequence=VSP_010089;
CC -!- SIMILARITY: Belongs to the nucleoporin interacting component (NIC)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97865.2; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK028864; BAC26158.1; -; mRNA.
DR EMBL; AK045380; BAC32337.1; -; mRNA.
DR EMBL; AK129055; BAC97865.2; ALT_FRAME; Transcribed_RNA.
DR EMBL; AK167105; BAE39254.1; -; mRNA.
DR EMBL; AK169693; BAE41309.1; -; mRNA.
DR EMBL; BC023140; AAH23140.1; -; mRNA.
DR EMBL; AJ505051; CAD43733.1; -; Other_RNA.
DR CCDS; CCDS22540.1; -. [Q8BJ71-1]
DR RefSeq; NP_765998.1; NM_172410.2. [Q8BJ71-1]
DR RefSeq; XP_006531437.1; XM_006531374.3.
DR RefSeq; XP_006531438.1; XM_006531375.3.
DR RefSeq; XP_006531439.1; XM_006531376.2. [Q8BJ71-2]
DR AlphaFoldDB; Q8BJ71; -.
DR SMR; Q8BJ71; -.
DR BioGRID; 214942; 24.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q8BJ71; 5.
DR MINT; Q8BJ71; -.
DR STRING; 10090.ENSMUSP00000105174; -.
DR iPTMnet; Q8BJ71; -.
DR PhosphoSitePlus; Q8BJ71; -.
DR SwissPalm; Q8BJ71; -.
DR REPRODUCTION-2DPAGE; IPI00222307; -.
DR REPRODUCTION-2DPAGE; IPI00410800; -.
DR EPD; Q8BJ71; -.
DR jPOST; Q8BJ71; -.
DR MaxQB; Q8BJ71; -.
DR PaxDb; Q8BJ71; -.
DR PeptideAtlas; Q8BJ71; -.
DR PRIDE; Q8BJ71; -.
DR ProteomicsDB; 287862; -. [Q8BJ71-1]
DR ProteomicsDB; 287863; -. [Q8BJ71-2]
DR Antibodypedia; 14851; 142 antibodies from 28 providers.
DR DNASU; 71805; -.
DR Ensembl; ENSMUST00000079961; ENSMUSP00000078878; ENSMUSG00000032939. [Q8BJ71-1]
DR Ensembl; ENSMUST00000109547; ENSMUSP00000105174; ENSMUSG00000032939. [Q8BJ71-1]
DR Ensembl; ENSMUST00000212824; ENSMUSP00000148700; ENSMUSG00000032939. [Q8BJ71-1]
DR GeneID; 71805; -.
DR KEGG; mmu:71805; -.
DR UCSC; uc009mvz.1; mouse. [Q8BJ71-1]
DR CTD; 9688; -.
DR MGI; MGI:1919055; Nup93.
DR VEuPathDB; HostDB:ENSMUSG00000032939; -.
DR eggNOG; KOG2168; Eukaryota.
DR GeneTree; ENSGT00390000016353; -.
DR HOGENOM; CLU_011846_1_0_1; -.
DR InParanoid; Q8BJ71; -.
DR OMA; LLMCGQF; -.
DR OrthoDB; 187731at2759; -.
DR PhylomeDB; Q8BJ71; -.
DR TreeFam; TF315118; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR BioGRID-ORCS; 71805; 22 hits in 72 CRISPR screens.
DR ChiTaRS; Nup93; mouse.
DR PRO; PR:Q8BJ71; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BJ71; protein.
DR Bgee; ENSMUSG00000032939; Expressed in somite and 254 other tissues.
DR ExpressionAtlas; Q8BJ71; baseline and differential.
DR Genevisible; Q8BJ71; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
DR InterPro; IPR007231; Nucleoporin_int_Nup93/Nic96.
DR PANTHER; PTHR11225; PTHR11225; 1.
DR Pfam; PF04097; Nic96; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Translocation; Transport.
FT CHAIN 1..819
FT /note="Nuclear pore complex protein Nup93"
FT /id="PRO_0000124783"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1F7"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010089"
FT CONFLICT 116
FT /note="E -> K (in Ref. 5; CAD43733)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="F -> Y (in Ref. 1; BAC32337)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="A -> V (in Ref. 4; AAH23140)"
FT /evidence="ECO:0000305"
FT CONFLICT 816..819
FT /note="VLMN -> LLSWEVH (in Ref. 1; BAC32337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 819 AA; 93281 MW; 747EA591189DAFAF CRC64;
MDTEGFGELL QQAEQLAAET EGISELPHVE RNLQEIQQAG ERLRSRTLTR TSQETADVKA
SVLLGSRGLD ISHISQRLES LSAATTFEPL EPVKDTDIQG FLKNEKDNAL LSAIEESRKR
TFGMAEEYHR ESMLVEWEQV KQRILHTLLA SGEDALDFTQ ESEPSYIGDV NPPGRSSLDS
IEMAYARQIY IYNEKIVSGH LQPNLVDLCA SVAELDDKSI SDMWAMVKQM TDVVLTPATD
ALKSRSSVEV RMDFVKQALG YLEQSYKNYT LVTVFGNLHQ AQLGGVPGTY QLVRSFLNIK
LPAPSPGLQD GEVEGHPVWA LIYYCMRCGD LLAASQVVSR AQHQLGEFKT WFQEYMNSKD
RRLSPATENK LRLHYRRALR NNTDPYKRAV YCIIGRCDIT DNQSEVADKT EDYLWLKLNQ
VCFDDDGTSS PQDRLTLSQF QKQLLEDYGE SHFTVNQQPF LYFQVLFLTA QFEAAIAFLF
RMERLRCHAV HVALVLFELK LLLKSSGQSA QLLSHEPGDP PCMRRLNFVR LLMLYTRKFE
STDPREALQY FYFLRDEKDS QGENMFLRCV SELVIESREF DMILGKLEND GSRKPGVIDK
FTSDTKPIIN KVASVAENKG LFEEAAKLYD LAKNADKVLE LMNKLLSPVV PQISAPQSNK
ERLKNMALSI AERYRAQGIS ANKFVDSTFY LLLDLITFFD EYHSGHIDRA FDIIDRLKLV
PLNQESVEER VAAFRNFSDE IRHNLSEVLL ATMNILFTQF KRLKGTSPSS ATRPQRVIED
RDSQLRSQAR ALITFAGMIP YRTSGDTNAR LVQMEVLMN
